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O48646 (GPX6_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial

Short name=AtGPX1
Short name=PHGPx
EC=1.11.1.12
Gene names
Name:GPX6
Synonyms:GPX1
Ordered Locus Names:At4g11600
ORF Names:T5C23.30
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione By similarity.

Catalytic activity

2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H2O.

Subcellular location

Mitochondrion Potential.

Tissue specificity

Expressed at a low but detectable level in leaves, stems, and flowers, but at a higher level in siliques and even higher in roots. Predominantly expressed in seeds. Ref.1 Ref.7

Induction

By salt stress, osmotic stress, cold treatment, and metals. Up-regulated by salicylic acid (SA), jasmonic acid (JA), abscisic acid (ABA) and auxin. Ref.1 Ref.6 Ref.7

Sequence similarities

Belongs to the glutathione peroxidase family.

Sequence caution

The sequence AAC09173.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAM66969.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA24226.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB39931.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB78203.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5454Mitochondrion Potential
Chain55 – 232178Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
PRO_0000013088

Sites

Active site1051 By similarity

Experimental info

Sequence conflict301S → SSSS Ref.1
Sequence conflict511S → Y Ref.6

Sequences

Sequence LengthMass (Da)Tools
O48646 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: 93F3084A8A331494

FASTA23225,584
        10         20         30         40         50         60 
MLRSSIRLLY IRRTSPLLRS LSSSSSSSSS KRFDSAKPLF NSHRIISLPI STTGAKLSRS 

        70         80         90        100        110        120 
EHSMAASSEP KSLYDFTVKD AKGNDVDLSI YKGKVLLIVN VASQCGLTNS NYTELAQLYE 

       130        140        150        160        170        180 
KYKGHGFEIL AFPCNQFGNQ EPGTNEEIVQ FACTRFKAEY PIFDKVDVNG DKAAPVYKFL 

       190        200        210        220        230 
KSSKGGLFGD GIKWNFAKFL VDKDGNVVDR FAPTTSPLSI EKDVKKLLGV TA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a cDNA encoding a putative glutathione peroxidase protein from Arabidopsis thaliana."
Bilodeau P., Luo M., Dennis E.S., Peacock W.J., Chaudhury A.M.
Plant Gene Register PGR98-047
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
Strain: cv. Landsberg erecta.
[2]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-232.
[6]"Putative phospholipid hydroperoxide glutathione peroxidase gene from Arabidopsis thaliana induced by oxidative stress."
Sugimoto M., Sakamoto W.
Genes Genet. Syst. 72:311-316(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-232, INDUCTION.
Strain: cv. Columbia.
[7]"Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated by abiotic stresses through diverse signaling pathways."
Rodriguez Milla M.A., Maurer A., Rodriguez Huete A., Gustafson J.P.
Plant J. 36:602-615(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF030132 mRNA. Translation: AAC09173.1. Different initiation.
AL049500 Genomic DNA. Translation: CAB39931.1. Different initiation.
AL161532 Genomic DNA. Translation: CAB78203.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE83029.1.
AY039863 mRNA. Translation: AAK63967.1.
AY077655 mRNA. Translation: AAL76133.1.
AY088647 mRNA. Translation: AAM66969.1. Different initiation.
AB001568 mRNA. Translation: BAA24226.1. Different initiation.
PIRT04207.
RefSeqNP_192897.2. NM_117229.3.
UniGeneAt.23184.

3D structure databases

ProteinModelPortalO48646.
SMRO48646. Positions 71-230.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid12064. 1 interaction.
IntActO48646. 2 interactions.
STRING3702.AT4G11600.1-P.

Protein family/group databases

PeroxiBase2502. AtGPx06.

Proteomic databases

PaxDbO48646.
PRIDEO48646.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G11600.1; AT4G11600.1; AT4G11600.
GeneID826765.
KEGGath:AT4G11600.

Organism-specific databases

GeneFarm2055. 163.
TAIRAT4G11600.

Phylogenomic databases

eggNOGCOG0386.
HOGENOMHOG000277054.
InParanoidO48646.
KOK00432.
OMARFAPLTK.
PhylomeDBO48646.

Gene expression databases

GenevestigatorO48646.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000889. Glutathione_peroxidase.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR11592. PTHR11592. 1 hit.
PfamPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFPIRSF000303. Glutathion_perox. 1 hit.
PRINTSPR01011. GLUTPROXDASE.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGPX6_ARATH
AccessionPrimary (citable) accession number: O48646
Secondary accession number(s): Q94BV3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 10, 2004
Last modified: May 14, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names